ID   STEL6_DROME             Reviewed;         172 AA.
AC   Q7KV22;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Stellate protein CG33246;
GN   Name=Ste:CG33246; ORFNames=CG33246;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH CKII-ALPHA.
RX   PubMed=7597082; DOI=10.1073/pnas.92.13.6067;
RA   Bozzetti M.P., Massari S., Finelli P., Meggio F., Pinna L.A., Boldyreff B.,
RA   Issinger O.G., Palumbo G., Ciriaco C., Bonaccorsi S., Pimpinelli S.;
RT   "The Ste locus, a component of the parasitic cry-Ste system of Drosophila
RT   melanogaster, encodes a protein that forms crystals in primary
RT   spermatocytes and mimics properties of the beta subunit of casein kinase
RT   2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:6067-6071(1995).
RN   [4]
RP   INDUCTION.
RX   PubMed=11513298; DOI=10.1007/s004120100136;
RA   Stapleton W., Das S., McKee B.D.;
RT   "A role of the Drosophila homeless gene in repression of Stellate in male
RT   meiosis.";
RL   Chromosoma 110:228-240(2001).
RN   [5]
RP   INDUCTION.
RX   PubMed=11470406; DOI=10.1016/s0960-9822(01)00299-8;
RA   Aravin A.A., Naumova N.M., Tulin A.V., Vagin V.V., Rozovsky Y.M.,
RA   Gvozdev V.A.;
RT   "Double-stranded RNA-mediated silencing of genomic tandem repeats and
RT   transposable elements in the D. melanogaster germline.";
RL   Curr. Biol. 11:1017-1027(2001).
CC   -!- FUNCTION: Unknown. In males lacking the Y chromosome, its strong
CC       overexpression leads to the appearance of proteinaceous star-shaped
CC       crystals in the primary spermatocytes causing meiotic drive, possibly
CC       by interfering with normal casein kinase 2 activity.
CC   -!- SUBUNIT: Interacts in vitro with the casein kinase 2 alpha subunit
CC       (CkII-alpha). The relevance of such interaction is however unclear in
CC       vivo. {ECO:0000269|PubMed:7597082}.
CC   -!- TISSUE SPECIFICITY: Probably not expressed in wild-type flies. In males
CC       lacking the Y chromosome, it is testis-specific and constitutes the
CC       main component of star-shaped crystals. {ECO:0000269|PubMed:7597082}.
CC   -!- INDUCTION: In wild-type flies, it is strongly down-regulated by double-
CC       stranded RNA (dsRNA) interference mediated by Su(Ste) transcripts. In
CC       males lacking the Y chromosome, the absence of Su(Ste) locus, relieves
CC       such down-regulation, explaining why it is strongly expressed.
CC       {ECO:0000269|PubMed:11470406, ECO:0000269|PubMed:11513298}.
CC   -!- MISCELLANEOUS: There are multiple copies of the stellate gene in fruit
CC       fly, encoding proteins that are extremely similar, which makes their
CC       individual characterization difficult. Thus, most experiments probably
CC       do not discriminate between the different members.
CC   -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AE014298; AAS65328.2; -; Genomic_DNA.
DR   RefSeq; NP_996422.2; NM_206699.2.
DR   AlphaFoldDB; Q7KV22; -.
DR   SMR; Q7KV22; -.
DR   STRING; 7227.FBpp0289372; -.
DR   PaxDb; Q7KV22; -.
DR   EnsemblMetazoa; FBtr0300095; FBpp0289372; FBgn0053246.
DR   GeneID; 2768905; -.
DR   KEGG; dme:Dmel_CG33246; -.
DR   UCSC; CG33246-RB; d. melanogaster.
DR   CTD; 2768905; -.
DR   FlyBase; FBgn0053246; Ste:CG33246.
DR   VEuPathDB; VectorBase:FBgn0053246; -.
DR   eggNOG; KOG3092; Eukaryota.
DR   GeneTree; ENSGT00390000003781; -.
DR   HOGENOM; CLU_034027_3_3_1; -.
DR   InParanoid; Q7KV22; -.
DR   PhylomeDB; Q7KV22; -.
DR   BioGRID-ORCS; 2768905; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 2768905; -.
DR   PRO; PR:Q7KV22; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Genevisible; Q7KV22; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005956; C:protein kinase CK2 complex; IDA:FlyBase.
DR   GO; GO:0019887; F:protein kinase regulator activity; IMP:FlyBase.
DR   GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IMP:FlyBase.
DR   Gene3D; 1.10.1820.10; -; 1.
DR   InterPro; IPR016149; Casein_kin_II_reg-sub_N.
DR   InterPro; IPR035991; Casein_kinase_II_beta-like.
DR   InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR   PANTHER; PTHR11740; PTHR11740; 1.
DR   Pfam; PF01214; CK_II_beta; 1.
DR   PRINTS; PR00472; CASNKINASEII.
DR   SMART; SM01085; CK_II_beta; 1.
DR   SUPFAM; SSF57798; SSF57798; 1.
DR   PROSITE; PS01101; CK2_BETA; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..172
FT                   /note="Stellate protein CG33246"
FT                   /id="PRO_0000068266"
SQ   SEQUENCE   172 AA;  19479 MW;  9A2AD5078307F69B CRC64;
     MSSSQNNNSS WIDWFLGIKG NQFLCRVPTD YVQDTFNQMG LEYFSEILDV ILKPVIDSSS
     GLLYGDGKKW YGMIHARYIR SERGLIAMHR KYMRGDFGSC PNISCDRQNT LPVGLSAVWG
     KSTVKIHCPR CKSNFYPKSD TQLDGAMFGP SFPDIFFSLL PNLTSPLDDP RT